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dc.contributor.authorMercurio, Arthur M.
dc.contributor.authorRabinovitz, Isaac
dc.contributor.authorShaw, Leslie M.
dc.date2022-08-11T08:08:02.000
dc.date.accessioned2022-08-23T15:39:57Z
dc.date.available2022-08-23T15:39:57Z
dc.date.issued2001-10-01
dc.date.submitted2010-11-12
dc.identifier.citationCurr Opin Cell Biol. 2001 Oct;13(5):541-5.
dc.identifier.pmid11544021
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26291
dc.description.abstractAlthough the involvement of alpha 6 beta 4, an integrin laminin receptor, in hemidesmosome organization has dominated the study of this integrin, recent studies are revealing novel functions for alpha 6 beta 4 in the migration of epithelial and carcinoma cells. The engagement of laminin by alpha 6 beta 4 can stabilize actin-rich protrusions and mediate traction forces necessary for cell movement. This integrin also has a significant impact on signaling molecules that stimulate migration and invasion, especially PI3-K and Rho GTPases. Activation of PI3-K by alpha 6 beta 4 enhances the formation of actin protrusions, and it may stimulate the function of other integrins, such as alpha 3 beta 1, that are also important for epithelial migration. Signaling through alpha 6 beta 4 may not always depend on the adhesive functions of this integrin, a possibility that has profound implications for migration and invasion because it implies that the ability of alpha 6 beta 4 to stimulate these processes is not limited to specific matrix environments.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11544021&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/S0955-0674(00)00249-0
dc.subjectAntigens, Surface
dc.subjectCell Movement
dc.subjectEpithelial Cells
dc.subjectIntegrins
dc.subjectCancer Biology
dc.subjectNeoplasms
dc.titleThe alpha 6 beta 4 integrin and epithelial cell migration
dc.typeJournal Article
dc.source.journaltitleCurrent Opinion in Cell Biology
dc.source.volume13
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cancerbiology_pp/207
dc.identifier.contextkey1640494
html.description.abstract<p>Although the involvement of alpha 6 beta 4, an integrin laminin receptor, in hemidesmosome organization has dominated the study of this integrin, recent studies are revealing novel functions for alpha 6 beta 4 in the migration of epithelial and carcinoma cells. The engagement of laminin by alpha 6 beta 4 can stabilize actin-rich protrusions and mediate traction forces necessary for cell movement. This integrin also has a significant impact on signaling molecules that stimulate migration and invasion, especially PI3-K and Rho GTPases. Activation of PI3-K by alpha 6 beta 4 enhances the formation of actin protrusions, and it may stimulate the function of other integrins, such as alpha 3 beta 1, that are also important for epithelial migration. Signaling through alpha 6 beta 4 may not always depend on the adhesive functions of this integrin, a possibility that has profound implications for migration and invasion because it implies that the ability of alpha 6 beta 4 to stimulate these processes is not limited to specific matrix environments.</p>
dc.identifier.submissionpathcancerbiology_pp/207
dc.contributor.departmentDepartment of Cancer Biology
dc.source.pages541-5


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